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Nanoscale Structural Organization of Insulin Fibril Polymorphs Revealed By Atomic Force Microscope Infrared Spectroscopy (AFM-IR).

08:00 EDT 12th July 2019 | BioPortfolio

Summary of "Nanoscale Structural Organization of Insulin Fibril Polymorphs Revealed By Atomic Force Microscope Infrared Spectroscopy (AFM-IR)."

Spontaneous aggregation of misfolded proteins typically results in formation morphologically and structurally different amyloid fibrils, protein aggregates that are strongly associated with various neurodegenerative disorders. Elucidation of structural organization of amyloid aggregates is crucial for the understanding of their role in onset and progression of these diseases. Using atomic force microscopy infrared spectroscopy (AFM-IR), we investigated structural organization of insulin fibrils. We found that aggregation of insulin results in formation of two structurally different fibril polymorphs. One fibril polymorph has a β-sheet core surrounded by primarily unordered protein secondary structure. This first fibril polymorph has β-sheet-rich surface, whereas the surface of the second fibril polymorph is primarily composed of the unordered protein. Using AFM-IR, we also revealed structural organization of insulin oligomers. Finally, we discovered a new pathway for amyloid fibril formation that is based on a fusion of several oligomers into the single fibril structure.

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This article was published in the following journal.

Name: Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
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Medical and Biotech [MESH] Definitions

A scleroprotein fibril consisting mostly of type III collagen. Reticulin fibrils are extremely thin, with a diameter of between 0.5 and 2 um. They are involved in maintaining the structural integrity in a variety of organs.

A syndrome with excessively high INSULIN levels in the BLOOD. It may cause HYPOGLYCEMIA. Etiology of hyperinsulinism varies, including hypersecretion of a beta cell tumor (INSULINOMA); autoantibodies against insulin (INSULIN ANTIBODIES); defective insulin receptor (INSULIN RESISTANCE); or overuse of exogenous insulin or HYPOGLYCEMIC AGENTS.

Diminished effectiveness of INSULIN in lowering blood sugar levels: requiring the use of 200 units or more of insulin per day to prevent HYPERGLYCEMIA or KETOSIS. It can be caused by the presence of INSULIN ANTIBODIES or the abnormalities in insulin receptors (RECEPTOR, INSULIN) on target cell surfaces. It is often associated with OBESITY; DIABETIC KETOACIDOSIS; INFECTION; and certain rare conditions. (from Stedman, 25th ed)

An insulin preparation that is designed to provide immediate and long term glycemic control in a single dosage. Biphasic insulin typically contains a mixture of REGULAR INSULIN or SHORT-ACTING INSULIN combined with a LONG-ACTING INSULIN.

A member of the alkali metals. It has an atomic symbol Cs, atomic number 50, and atomic weight 132.91. Cesium has many industrial applications, including the construction of atomic clocks based on its atomic vibrational frequency.

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